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Information on EC 1.1.1.335 - UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase

for references in articles please use BRENDA:EC1.1.1.335

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IUBMB Comments

This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalysing the next step the pathway (EC 2.6.1.98, UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase). The enzyme also possesses an EC 1.1.99.2 (L-2-hydroxyglutarate dehydrogenase) activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD+. The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD+ as tightly and do not require 2-oxoglutarate to function.

The enzyme appears in viruses and cellular organisms

Synonyms
PGN_0168, WblA, WbpB, WlbA, more

SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
WbpB
-
-
-
-
PATHWAY SOURCE
PATHWAYS
MetaCyc
UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronate biosynthesis
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-2-amino-2-deoxy-alpha-D-glucuronate:NAD+ 3-oxidoreductase
This enzyme participates in the biosynthetic pathway for UDP-alpha-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-alpha-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalysing the next step the pathway (EC 2.6.1.98, UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase). The enzyme also possesses an EC 1.1.99.2 (L-2-hydroxyglutarate dehydrogenase) activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD+. The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD+ as tightly and do not require 2-oxoglutarate to function.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Gene Links
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q72KX8_THET2
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
310
0
34590
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the enzyme in a complex with NAD(H) and 2-oxoglutarate, and the enzyme in a complex with NAD(H) and its substrate UDP-N-acetyl-D-glucosaminuronic acid, to 1.45 A and 2.0 A resolution, respectively. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft. Residues Lys101 and His185 most likely play key roles in catalysis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thoden, J.; Holden, H.
Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid
Biochemistry
49
7939-7948
2010
Thermus thermophilus (Q72KX8), Pseudomonas aeruginosa (G3XD23)
Manually annotated by BRENDA team